ID A0A1V2Q2H5_9PSEU Unreviewed; 615 AA.
AC A0A1V2Q2H5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:ONI82378.1};
GN ORFNames=ALI22I_40465 {ECO:0000313|EMBL:ONI82378.1};
OS Saccharothrix sp. ALI-22-I.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI82378.1, ECO:0000313|Proteomes:UP000188617};
RN [1] {ECO:0000313|EMBL:ONI82378.1, ECO:0000313|Proteomes:UP000188617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI82378.1,
RC ECO:0000313|Proteomes:UP000188617};
RX PubMed=28087533;
RA Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA Kuske C.R.;
RT "Polysaccharide degradation capability of Actinomycetales soil isolates
RT from a semi-arid grassland of the Colorado Plateau.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ONI82378.1}.
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DR EMBL; MTQP01000068; ONI82378.1; -; Genomic_DNA.
DR RefSeq; WP_077010847.1; NZ_MTQP01000068.1.
DR AlphaFoldDB; A0A1V2Q2H5; -.
DR STRING; 1933778.ALI22I_40465; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000188617; Unassembled WGS sequence.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR030817; Myo_inos_IolD.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ONI82378.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188617};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 218..350
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 433..569
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 615 AA; 65862 MW; 3D574F1524A68855 CRC64;
MRLTTAQALV RWLLAQRTEL PDNTEGPLFP GVFAIFGHGN VLGLGNALEE FRTEIPVWRG
HNEQGMALAA VGIGKATHRR QVGVATSSIG PGALNMVTAA GVAHANRLPL LLLPGDTFTS
RAPDPVLQQV EHYGDPTTTV NDAFRAVSRY FDRITRPEQL LNTLPQVARV LTDPADCGPV
TLALPQDVQA ESFDFPDALF TPVVHRPTRP RPDIRALTEA AETLRRARKP LLVLGGGVRY
SRAAGRAIRF AEQHAIPIAE TTAGRTLVPH DHPLHAGPLG ITGSTSANVL AAEADVVLAV
GTRLQDFTTA SWTVFAPDVR IVSLNAARYD AVKHGALSLV ADADEGLREL TDELGDWQAD
ATWAARAGQE RAKWDAHIEG LRAPATTPTY AQVVGVVNDL STPEDYVMTA SGGMPGELIG
GWRAIGEASM DVEYGFSCMG YELAGAWGAA IARPDGVVTT LLGDGSYLML NSELFSAAFA
GHGFVAVVCD NDGYAVIHRL QTGQGGAGFN NLYDDVRTAH ARPPRTDFAA HAASMGCATF
PVDDIKDLAE AYRKAREVAK TEHRPAVVVI RTHPSSWTEA GAWWEVGVPE VAHRPEITAA
HQEVATGKAK QIRYL
//
